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Literature summary for 4.2.1.22 extracted from

  • Weeks, C.L.; Singh, S.; Madzelan, P.; Banerjee, R.; Spiro, T.G.
    Heme regulation of human cystathionine beta-synthase activity: insights from fluorescence and Raman spectroscopy (2009), J. Am. Chem. Soc., 131, 12809-12816.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
truncated protein lacking the C-terminal domain is expressed Homo sapiens

Protein Variants

Protein Variants Comment Organism
DELTAC studies are carried out using a truncated protein lacking the C-terminal domain. kcat increases by a factor of 4 and the responsiveness to S-adenosyl-L-methionine is lost. The C-terminal domain is involved in the aggregation of the full-length protein, which exists as a mixture of tetramer and higher oligomers, while the 45 kDa truncated form lacking the C-terminal domain is a dimer Homo sapiens
R266M enzyme is inactivated, pyridoxal 5'-phosphate is displaced by breaking the salt bridge between Cys52 and Arg266 Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
CO CO binding is found to induce a tautomeric shift of the pyridoxal 5'-phosphate from the ketoenamine to the enolimine form. The ketoenamine is key to pyridoxal 5'-phosphate reactivity because its imine C-N bond is protonated, facilitating attack by the nucleophilic substrate, serine Homo sapiens
NO
-
Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
45000
-
molecular weight of the truncated protein lacking the C-terminal domain Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Subunits

Subunits Comment Organism
dimer
-
Homo sapiens

Synonyms

Synonyms Comment Organism
CBS
-
Homo sapiens
cystathionine beta-synthase
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
heme CO binding displaces Cys52 from the heme Homo sapiens
pyridoxal 5'-phosphate
-
Homo sapiens